macromolecules part b
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what is a nucleic acid?
• genetic material of the cell (cell fxn, replication, and genetic info)
what monomer makes up nucleic acids and what bonds the monomers together?
• nucleotides (sugar (deoxy or ribo) phosphate backbone and nitrogenous bases) • phosphodiester bonds !
what bonds form between nitrogenous bases of a nucleotide
Hydrogen bonds (covalent)`
what are the three chemical differences between DNA and RNA
-sugar used in backbones (deoxyribose or ribose) - 3D structure (RNA bonds internally, single stranded) - Uracil pyrimidine base instead of Thymine
DNA is a directional molecule what does this mean
the 3’ (attached to OH group at end of DNA) bonds with the 5’ end (attached to the terminal phosphate) of each strand
purines vs pyrimidines
PURINES; A&G- one pentose PYRIMIDINES; T(U)&C- two carbon rings
which nitrogenous base bonds with which, and why?
G-C and A-T (because purines and pyrimidines are structurally different and are unable to form sufficient bonds within like pairs)
how are proteins formed
amino acids are bonded together by peptide bonds to form linear polypeptide strands which fold and coil into itself to become a protein
what are examples of polypeptides
hemoglobin, collagen, and insulin
what are the four levels of protein structure? (+ bonds of each)
primary: unique order of amino acids (peptide) secondary: folding of polypeptide (H-bonds b/w carboxyl and amino) tertiary: overall folded 3D shape of polypeptide [protein formed] (H-bonds, ionic bonds, hydrophobic interactions, disulfide bonds in cystine) quaternary: multiple polypeptides together (same bonds as tertiary; h, ionic, disulfide, hydrophobic)
what are polypeptides (structure + fxn)
fxn: enzymes, transport &structural proteins, hormones, receptors etc) structure: long peptide bonded chain of amino acids made up of an amino group, R group, and carboxyl)
what does it mean for polypeptides to be directional?
folded chain only bonds carboxyl ends of amino acids to amino ends of others (creating and limiting unique shape)
what are the differences between denaturing and degrading a protein?
degrade; permanent damage of primary structure, no fxn left cant be reversed denature; non permanent damage of secondary, tertiary, and quaternary structures, protein can’t fxn